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J. Biol. Chem., Vol. 276, Issue 24, 21046-21052, June 15, 2001
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From the Departments of K-Cl cotransport (KCC) is activated by nitric
oxide donors and appears to be regulated by the cGMP signaling
pathway. Expression of KCC mRNAs (KCC1-KCC4) in rat vascular
smooth muscle cells (VSMCs) is unknown. We have reported the presence
of KCC1 and KCC3 mRNAs in primary cultures of VSMCs by specific
reverse transcription-polymerase chain reaction. KCC2 mRNA appeared
at extremely low levels. KCC4 mRNA was undetectable.
Semiquantitative reverse transcription-polymerase chain reaction
revealed a 2:1 KCC1/KCC3 mRNA ratio in VSMCs. Depletion of protein
kinase G (PKG)-1 from VSMCs did not change KCC3 mRNA expression.
Analogous results were obtained with PKG-1-catalytic domain- and
vector only-transfected VSMCs lacking endogenous PKG, suggesting no
involvement of PKG-1 in the maintenance of basal KCC3 mRNA
expression. However, 8-bromo-cGMP, a PKG stimulator, acutely increased
KCC3 mRNA expression in a concentration- and time-dependent fashion; this effect was blocked by the PKG
inhibitor KT5823 but not by actinomycin D. These findings show that
VSMCs express mainly two mRNA isoforms, KCC1 and KCC3, and suggest
that PKG participates post-transcriptionally in the acute KCC3 mRNA regulation. The role of KCC3 on cell volume and electrolyte homeostasis in response to PKG modulators remains to be determined.
Protein Kinase G Regulates Potassium Chloride Cotransporter-3
Expression in Primary Cultures of Rat Vascular Smooth Muscle Cells*
,
Pharmacology and Toxicology
and ¶ Physiology and Biophysics, Wright State University, School
of Medicine, Dayton, Ohio 45435-0002 and the § Department of
Pathology, Division of Molecular and Cellular Pathology, University of
Alabama at Birmingham, Birmingham, Alabama 35294
*
This work was supported by National American Heart
Association Grant 0050451N, by a Wright State University Pruet Seed
grant, and by Wright State University Research Challenge Program
99-623-10. Part of this work has been presented in abstract form (34).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Pharmacology and Toxicology, Wright State University, School of
Medicine, 3640 Colonel Glenn Hwy., Biological Science Bldg., Room
152-6, Dayton, OH 45435-0002. Tel.: 937-775-2104; Fax: 937-775-3769; E-mail: norma.adragna@wright.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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